We are continuing to pursue our studies on the conformation of the myelin basic protein (BP) by 1) circular dichroism spectroscopy, 2) immunological reactions, 3) chemical cross-linking, and 4) nuclear magnetic resonance spectroscopy. In addition, we are 5) isolating peptic fragments of the BP which contain in vivo phosphorylated serine and threonine residues for use in preparing antibodies specific to the phosphorylation sites.